5.4.3.8	additional information	during the first half of the reaction pyridoxamine 5'-phosphate is converted to pyridoxal 5'-phosphate, while pyridoxamine 5'-phosphate is regenerated in the second half of the reaction upon 5-aminolevulinate formation	746660	
5.4.3.8	additional information	in both the pyridoxamine 5'-phosphate- and pyridoxal 5'-phosphate-bound structures, the gating loops are well-defined in electron density and are in the ordered open conformation. The conformation of the gating loop is symmetrical	747005	
5.4.3.8	pyridoxal 5'-phosphate	-	649844, 653764	
5.4.3.8	pyridoxal 5'-phosphate	a pyridoxamine 5'-phosphate (PMP)/pyridoxal 5'-phosphate (PLP)-dependent enzyme, binding structure with a Schiff base linkage between the cofactor and the epsilon-amino group of Lys286, overview	747005	
5.4.3.8	pyridoxal 5'-phosphate	a pyridoxamine 5'-phosphate (PMP)/pyridoxal 5'-phosphate (PLP)-dependent enzyme, binding structure, overview	746660	
5.4.3.8	pyridoxal 5'-phosphate	acts as cofactor and stimulates	3438	
5.4.3.8	pyridoxal 5'-phosphate	cofactor is bound by a Schiff base to the protein	3435	
5.4.3.8	pyridoxal 5'-phosphate	dependent on	703619, 714041, 716103	
5.4.3.8	pyridoxal 5'-phosphate	dependent on, during the catalytic cycle, the cofactor undergoes conversion from pyridoxamine 5'-phosphate to pyridoxal 5'-phosphate, conformational changes and binding structures, overview	727125	
5.4.3.8	pyridoxal 5'-phosphate	pyridoxal 5'-phosphate binding site	3444	
5.4.3.8	pyridoxal 5'-phosphate	required	3436	
5.4.3.8	pyridoxamine 5'-phosphate	a pyridoxamine 5'-phosphate (PMP)/pyridoxal 5'-phosphate (PLP)-dependent enzyme, binding structure, overview	746660, 747005	
5.4.3.8	pyridoxamine 5'-phosphate	cofactor	3440	
5.4.3.8	pyridoxamine 5'-phosphate	conversion into the active pyridoxamine-phosphate form of enzyme in an exponential process	3442	
5.4.3.8	pyridoxamine 5'-phosphate	dependent on	703619, 714041	
5.4.3.8	pyridoxamine 5'-phosphate	only the pyridoxamine form of the enzyme is active	3439	
5.4.3.8	pyridoxamine 5'-phosphate	stimulates	3429	
5.4.3.8	pyridoxamine 5'-phosphate	the pyridoxal-phosphate form of the enzyme and the pyridoxamine-phosphate form of the enzyme are similarly active	3441	
5.4.3.8	vitamin B6	subunits show asymmetry in cofactor binding	3445	
5.4.3.8	vitamin B6	wild-type enzyme and gabaculine-resistant mutant enzyme contain vitamin B6	3430